Molecular weight determination of protein-dodecyl sulfate complexes by gel electrophoresis in a discontinuous buffer system.
Molecular weight determination of protein-dodecyl sulfate complexes by gel electrophoresis in a discontinuous buffer system.
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在不连续缓冲系统中通过凝胶电泳测定蛋白质-十二烷基硫酸盐复合物的分子量。
DOI：
10.1016/s0021-9258(18)61792-2
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发表时间：
1971
期刊：
影响因子：
--
通讯作者：
D. Neville
中科院分区：
文献类型：
--
作者：
D. Neville
本文介绍了十二烷基硫酸钠（SDS）凝胶电泳和不连续缓冲液电泳相结合的方法和结果。SDS凝胶系统利用硫酸盐-硼酸盐不连续性，其在2，300至320，000道尔顿的范围内堆积和分解蛋白质-SDS复合物，提供高分辨率分级分离。通过计算Ferguson图的阻滞系数和表观自由迁移率，研究了蛋白质-SDS复合物的性质。表观自由迁移率近似恒定，从而在相对迁移率的对数和延迟系数之间建立线性关系。的阻滞系数显示在经验和理论上是一个统一的函数的分子量的蛋白质-SDS复合物在指定的范围内，提供了一个基本原理确定分子量的相对迁移率的负对数对分子量的曲线。
This report describes methods and results obtained by combining the techniques of sodium dodecyl sulfate (SDS) gel electrophoresis and electrophoresis in discontinuous buffer systems. The SDS gel system utilizes a sulfate-borate discontinuity which stacks and unstacks protein-SDS complexes over a range of 2,300 to 320,000 daltons, providing high resolution fractionation. The properties of protein-SDS complexes are investigated by calculating retardation coefficients and apparent free mobilities from Ferguson plots. Apparent free mobilities are approximately constant, establishing a linear relationship between the logarithm of the relative mobility and the retardation coefficient. The retardation coefficient is shown both empirically and theoretically to be a uniform function of molecular weight of protein-SDS complexes over specified ranges, providing a rationale for determining molecular weight from plots of the negative logarithm of relative mobility against molecular weight.